Protein fibrillogenesis

Walsh DM, Hartley DM, Kusomoto Y, Fezoui Y, Condron MM, Lomakin A, Benedek GB, Selkoe DJ, Teplow DB. Amyloid fi-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J Biol Chem 1999 274 25949-25952. 

Pandya, M. J., Spooner, G. M., Sunde, M., Thorpe, J. R., Rodger, A., and Woolfson, D. N. (2000). Sticky-end assembly of a designed peptide fiber provides insight into protein fibrillogenesis. Biochemistry 39, 8728-8734. 

Kirkitadze MD, Condron MM, Teplow DB. Identification and characterization of key kinetic intermediates in amyloid fS-protein fibrillogenesis J. Mol. Biol. 2001 312 1103-1119. 

Walsh DM, et al. Amyloid beta -protein fibrillogenesis. Structure 38. and biological activity of protofibrUlar intermediates. J. Biol. 

G. B. Bebdek, D. J. Selkoe, and D. B. Teplow,/. Biol. Chem., 274, 25945 (1999). Amyloid Beta-protein Fibrillogenesis Structure and Biological Activity of Protofibrillar Intermediates. 

Yamamoto N, Matsubara T, Sato T, Yanagisawa K. Age-dependent high-density clustering of GMl ganglioside at presynaptic neuritic terminals promotes amyloid beta-protein fibrillogenesis. Biochim Biophys Acta. 2008 1778(12) 2717-2726. 

Lansbury P T 1999 Evolution of amyloids What normal protein folding oan tell us about fibrillogenesis and disease Proc. Nati Acad. Sci. (USA) 96 3342-4... 

Lomakin A, Teplow DB, Kirschner DA, Benedek GB. Kinetic theory of fibrillogenesis of amyloid beta-protein. Proc Natl Acad Sci USA 1997 94 7942-7947. 

Tau protein interacts with many other proteins that can contribute to abnormal fibrillogenesis. One example is a-synuclein, which induces fibrillization of tau. Coincubation of a-synnclein and tau synergistically promotes fibrillization of both proteins in vitro. Mice with a-synuclein mutation or a tau mutation exhibit filamen-tons inclusions of both proteins, which are abundant neuronal proteins that normally adopt an nnfolded conformation but polymerize into amyloid fibrils in... 

Hedbom E, Heinegard D. Interaction of a 59-kDa connective tissue matrix protein with collagen I and collagen II. J Biol Chem 1989 264 6898-6905. Neame PJ, Kay CJ, McQuillan DJ, Beales MP, Hassell JR. Independent modulation of collagen fibrillogenesis by decorin and lumican. Cell Mol Life Sci 2000 57 859-863. 

Florio T, Paludi D, Villa V, Principe DR, Corsaro A, Millo E, Damonte G, D Arrigo C, Russo C, Schettini G, Aceto A (2003) Contribution of two conserved glydne residues to fibrillogenesis of the 106-126 prion protein fragment. Evidence that a soluble variant of the 106-126 peptide is neurotoxic. J Neurochem 85 62-72... 

Hamodrakas SJ, Hoenger A, Iconomidou VA (2004) Amyloid fibrillogenesis of silkmoth chorion protein peptide-analogues via a liquid-crystalhne intermediate phase. J Struct Biol 145 226-235... 

Fibrin, a biopolymer similar to collagen, is involved in the natural blood-dotting process. Fibrinogen, which is a 360 kDa protein, composed of three pairs of polypeptide chains is the source of fibrin. The structure of fibrin can be divided into three major sections consisting of a central domain composed of fibrinopeptide E with two pairs of fibrinopeptide A and B molecules and two terminal domains of fibrinopeptide D. Spontaneous fibrillogenesis is the formation of a linear fibril by... 

---